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Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]

 TGFB1_HUMAN             Reviewed;         390 AA.
P01137; A8K792; Q9UCG4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
16-OCT-2019, entry version 249.
RecName: Full=Transforming growth factor beta-1 proprotein;
Contains:
RecName: Full=Latency-associated peptide {ECO:0000305|PubMed:2982829, ECO:0000305|PubMed:3162913, ECO:0000305|PubMed:7737999, ECO:0000305|PubMed:8471846};
Short=LAP;
Contains:
RecName: Full=Transforming growth factor beta-1 {ECO:0000305|PubMed:2982829, ECO:0000305|PubMed:3162913, ECO:0000305|PubMed:7737999, ECO:0000305|PubMed:8471846};
Short=TGF-beta-1;
Flags: Precursor;
Name=TGFB1 {ECO:0000312|HGNC:HGNC:11766}; Synonyms=TGFB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3470709; DOI=10.1093/nar/15.7.3188;
Derynck R., Rhee L., Chen E.Y., van Tilburg A.;
"Intron-exon structure of the human transforming growth factor-beta
precursor gene.";
Nucleic Acids Res. 15:3188-3189(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PRO-10 AND PRO-25.
PubMed=3861940; DOI=10.1038/316701a0;
Derynck R., Jarrett J.A., Chen E.Y., Eaton D.H., Bell J.R.,
Assoian R.K., Roberts A.B., Sporn M.B., Goeddel D.V.;
"Human transforming growth factor-beta complementary DNA sequence and
expression in normal and transformed cells.";
Nature 316:701-705(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Duodenum, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 279-390.
TISSUE=Carcinoma;
Urushizaki Y., Niitsu Y., Terui T., Koshida Y., Mahara K., Kohgo Y.,
Urushizaki I., Takahashi Y., Ito H.;
"Cloning and expression of the gene for human transforming growth
factor-beta in Escherichia coli.";
Tumor Res. 22:41-55(1987).
[8]
PROTEIN SEQUENCE OF 279-329.
TISSUE=Urinary bladder carcinoma;
PubMed=8471846; DOI=10.1006/prep.1993.1019;
Bourdrel L., Lin C.-H., Lauren S.L., Elmore R.H., Sugarman B.J.,
Hu S., Westcott K.R.;
"Recombinant human transforming growth factor-beta 1: expression by
Chinese hamster ovary cells, isolation, and characterization.";
Protein Expr. Purif. 4:130-140(1993).
[9]
PROTEIN SEQUENCE OF 279-301.
PubMed=2982829;
Massague J., Like B.;
"Cellular receptors for type beta transforming growth factor. Ligand
binding and affinity labeling in human and rodent cell lines.";
J. Biol. Chem. 260:2636-2645(1985).
[10]
PROTEIN SEQUENCE OF 30-42 AND 279-290, AND GLYCOSYLATION.
PubMed=3162913;
Miyazono K., Hellman U., Wernstedt C., Heldin C.H.;
"Latent high molecular weight complex of transforming growth factor
beta 1. Purification from human platelets and structural
characterization.";
J. Biol. Chem. 263:6407-6415(1988).
[11]
PROTEIN SEQUENCE OF 279-283, AND PROTEOLYTIC CLEAVAGE.
PubMed=7737999; DOI=10.1074/jbc.270.18.10618;
Dubois C.M., Laprise M.H., Blanchette F., Gentry L.E., Leduc R.;
"Processing of transforming growth factor beta 1 precursor by human
furin convertase.";
J. Biol. Chem. 270:10618-10624(1995).
[12]
GLYCOSYLATION.
PubMed=2493139; DOI=10.1038/338158a0;
Miyazono K., Heldin C.H.;
"Role for carbohydrate structures in TGF-beta 1 latency.";
Nature 338:158-160(1989).
[13]
INTERACTION WITH LTBP1.
PubMed=2022183; DOI=10.1002/j.1460-2075.1991.tb08049.x;
Miyazono K., Olofsson A., Colosetti P., Heldin C.H.;
"A role of the latent TGF-beta 1-binding protein in the assembly and
secretion of TGF-beta 1.";
EMBO J. 10:1091-1101(1991).
[14]
INTERACTION WITH LTBP1, AND MUTAGENESIS OF CYS-33.
PubMed=8617200; DOI=10.1002/j.1460-2075.1996.tb00355.x;
Saharinen J., Taipale J., Keski-Oja J.;
"Association of the small latent transforming growth factor-beta with
an eight cysteine repeat of its binding protein LTBP-1.";
EMBO J. 15:245-253(1996).
[15]
INTERACTION WITH LTBP1.
PubMed=8939931; DOI=10.1074/jbc.271.47.29891;
Gleizes P.E., Beavis R.C., Mazzieri R., Shen B., Rifkin D.B.;
"Identification and characterization of an eight-cysteine repeat of
the latent transforming growth factor-beta binding protein-1 that
mediates bonding to the latent transforming growth factor-beta1.";
J. Biol. Chem. 271:29891-29896(1996).
[16]
REVIEW.
PubMed=9150447; DOI=10.1038/ki.1997.188;
Munger J.S., Harpel J.G., Gleizes P.E., Mazzieri R., Nunes I.,
Rifkin D.B.;
"Latent transforming growth factor-beta: structural features and
mechanisms of activation.";
Kidney Int. 51:1376-1382(1997).
[17]
INTERACTION WITH DPT.
PubMed=9895299; DOI=10.1042/bj3370537;
Okamoto O., Fujiwara S., Abe M., Sato Y.;
"Dermatopontin interacts with transforming growth factor beta and
enhances its biological activity.";
Biochem. J. 337:537-541(1999).
[18]
TISSUE SPECIFICITY.
PubMed=11746498; DOI=10.1002/jcb.1249;
Shur I., Lokiec F., Bleiberg I., Benayahu D.;
"Differential gene expression of cultured human osteoblasts.";
J. Cell. Biochem. 83:547-553(2001).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[20]
INTERACTION WITH CD109.
PubMed=16754747; DOI=10.1096/fj.05-5229fje;
Finnson K.W., Tam B.Y.Y., Liu K., Marcoux A., Lepage P., Roy S.,
Bizet A.A., Philip A.;
"Identification of CD109 as part of the TGF-beta receptor system in
human keratinocytes.";
FASEB J. 20:1525-1527(2006).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[22]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH ASPN.
PubMed=17827158; DOI=10.1074/jbc.m700522200;
Nakajima M., Kizawa H., Saitoh M., Kou I., Miyazono K., Ikegawa S.;
"Mechanisms for asporin function and regulation in articular
cartilage.";
J. Biol. Chem. 282:32185-32192(2007).
[23]
FUNCTION, AND INTERACTION WITH LRRC32.
PubMed=19750484; DOI=10.1002/eji.200939684;
Stockis J., Colau D., Coulie P.G., Lucas S.;
"Membrane protein GARP is a receptor for latent TGF-beta on the
surface of activated human Treg.";
Eur. J. Immunol. 39:3315-3322(2009).
[24]
FUNCTION, INTERACTION WITH LRRC32, AND MUTAGENESIS OF CYS-33.
PubMed=22278742; DOI=10.1091/mbc.e11-12-1018;
Wang R., Zhu J., Dong X., Shi M., Lu C., Springer T.A.;
"GARP regulates the bioavailability and activation of TGFbeta.";
Mol. Biol. Cell 23:1129-1139(2012).
[25]
FUNCTION, AND INTERACTION WITH LRRC32.
PubMed=19651619; DOI=10.1073/pnas.0901944106;
Tran D.Q., Andersson J., Wang R., Ramsey H., Unutmaz D., Shevach E.M.;
"GARP (LRRC32) is essential for the surface expression of latent TGF-
beta on platelets and activated FOXP3+ regulatory T cells.";
Proc. Natl. Acad. Sci. U.S.A. 106:13445-13450(2009).
[26]
INTERACTION WITH HSP90AB1.
PubMed=20599762; DOI=10.1016/j.bbrc.2010.06.112;
Suzuki S., Kulkarni A.B.;
"Extracellular heat shock protein HSP90beta secreted by MG63
osteosarcoma cells inhibits activation of latent TGF-beta1.";
Biochem. Biophys. Res. Commun. 398:525-531(2010).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
FUNCTION.
PubMed=25310401; DOI=10.1371/journal.pone.0108528;
Chen Q., Lee C.E., Denard B., Ye J.;
"Sustained induction of collagen synthesis by TGF-beta requires
regulated intramembrane proteolysis of CREB3L1.";
PLoS ONE 9:E108528-E108528(2014).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[30]
FUNCTION.
PubMed=25893292; DOI=10.1038/onc.2015.100;
Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H.,
Lee J.H.;
"Syntenin regulates TGF-beta1-induced Smad activation and the
epithelial-to-mesenchymal transition by inhibiting caveolin-mediated
TGF-beta type I receptor internalization.";
Oncogene 35:389-401(2016).
[31]
REVIEW.
PubMed=27252363; DOI=10.1101/cshperspect.a021907;
Robertson I.B., Rifkin D.B.;
"Regulation of the bioavailability of TGF-beta and TGF-beta-related
proteins.";
Cold Spring Harb. Perspect. Biol. 8:0-0(2016).
[32]
FUNCTION, AND INTERACTION WITH NRROS.
PubMed=29909984; DOI=10.1016/j.cell.2018.05.027;
Qin Y., Garrison B.S., Ma W., Wang R., Jiang A., Li J., Mistry M.,
Bronson R.T., Santoro D., Franco C., Robinton D.A., Stevens B.,
Rossi D.J., Lu C., Springer T.A.;
"A milieu molecule for TGF-beta required for microglia function in the
nervous system.";
Cell 174:156-171(2018).
[33]
FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN IBDIMDE, VARIANTS
IBDIMDE CYS-45; CYS-110 AND ARG-387, AND CHARACTERIZATION OF VARIANTS
IBDIMDE CYS-45; CYS-110 AND ARG-387.
PubMed=29483653; DOI=10.1038/s41588-018-0063-6;
Kotlarz D., Marquardt B., Baroey T., Lee W.S., Konnikova L.,
Hollizeck S., Magg T., Lehle A.S., Walz C., Borggraefe I., Hauck F.,
Bufler P., Conca R., Wall S.M., Schumacher E.M., Misceo D.,
Frengen E., Bentsen B.S., Uhlig H.H., Hopfner K.P., Muise A.M.,
Snapper S.B., Stroemme P., Klein C.;
"Human TGF-beta1 deficiency causes severe inflammatory bowel disease
and encephalopathy.";
Nat. Genet. 50:344-348(2018).
[34]
STRUCTURE BY NMR OF 279-390.
PubMed=8424942; DOI=10.1021/bi00055a021;
Archer S.J., Bax A., Roberts A.B., Sporn M.B., Ogawa Y., Piez K.A.,
Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J.,
Torchia D.A.;
"Transforming growth factor beta 1: NMR signal assignments of the
recombinant protein expressed and isotopically enriched using Chinese
hamster ovary cells.";
Biochemistry 32:1152-1163(1993).
[35]
STRUCTURE BY NMR OF 279-390.
PubMed=8424943; DOI=10.1021/bi00055a022;
Archer S.J., Bax A., Roberts A.B., Sporn M.B., Ogawa Y., Piez K.A.,
Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J.,
Torchia D.A.;
"Transforming growth factor beta 1: secondary structure as determined
by heteronuclear magnetic resonance spectroscopy.";
Biochemistry 32:1164-1171(1993).
[36]
STRUCTURE BY NMR OF 279-390.
PubMed=8679613; DOI=10.1021/bi9604946;
Hinck A.P., Archer S.J., Qian S.W., Roberts A.B., Sporn M.B.,
Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J.,
Torchia D.A.;
"Transforming growth factor beta 1: three-dimensional structure in
solution and comparison with the X-ray structure of transforming
growth factor beta 2.";
Biochemistry 35:8517-8534(1996).
[37] {ECO:0000244|PDB:3KFD}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 279-390 IN COMPLEX WITH
TGFBR1 AND TGFBR2, FUNCTION, SUBUNIT, AND DISULFIDE BONDS.
PubMed=20207738; DOI=10.1074/jbc.m109.079921;
Radaev S., Zou Z., Huang T., Lafer E.M., Hinck A.P., Sun P.D.;
"Ternary complex of transforming growth factor-beta1 reveals isoform-
specific ligand recognition and receptor recruitment in the
superfamily.";
J. Biol. Chem. 285:14806-14814(2010).
[38] {ECO:0000244|PDB:4KV5}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 279-390, SUBUNIT, AND
DISULFIDE BONDS.
PubMed=25209176; DOI=10.1002/pro.2548;
Moulin A., Mathieu M., Lawrence C., Bigelow R., Levine M., Hamel C.,
Marquette J.P., Le Parc J., Loux C., Ferrari P., Capdevila C.,
Dumas J., Dumas B., Rak A., Bird J., Qiu H., Pan C.Q., Edmunds T.,
Wei R.R.;
"Structures of a pan-specific antagonist antibody complexed to
different isoforms of TGFbeta reveal structural plasticity of
antibody-antigen interactions.";
Protein Sci. 23:1698-1707(2014).
[39] {ECO:0000244|PDB:5FFO}
X-RAY CRYSTALLOGRAPHY (3.49 ANGSTROMS) OF 34-390 IN COMPLEX WITH ITGAV
AND ITGB6, FUNCTION, INTERACTION WITH ITGAV AND ITGB6, SUBUNIT,
DISULFIDE BOND, GLYCOSYLATION AT ASN-82, AND MUTAGENESIS OF GLU-75;
LEU-158; LEU-160; PRO-193; 232-LEU--ILE-236; 234-VAL--ILE-236;
ASN-237; ASN-254 AND 257-PHE--LEU-260.
PubMed=28117447; DOI=10.1038/nature21035;
Dong X., Zhao B., Iacob R.E., Zhu J., Koksal A.C., Lu C., Engen J.R.,
Springer T.A.;
"Force interacts with macromolecular structure in activation of TGF-
beta.";
Nature 542:55-59(2017).
[40] {ECO:0000244|PDB:5VQP}
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 30-390, SUBUNIT, DISULFIDE
BONDS, AND MUTAGENESIS OF ARG-278.
PubMed=29109152; DOI=10.1074/jbc.m117.809657;
Zhao B., Xu S., Dong X., Lu C., Springer T.A.;
"Prodomain-growth factor swapping in the structure of pro-TGF-beta1.";
J. Biol. Chem. 293:1579-1589(2018).
[41]
VARIANT PRO-10.
PubMed=9783545; DOI=10.1359/jbmr.1998.13.10.1569;
Yamada Y., Miyauchi A., Goto J., Takagi Y., Okuizumi H., Kanematsu M.,
Hase M., Takai H., Harada A., Ikeda K.;
"Association of a polymorphism of the transforming growth factor-beta1
gene with genetic susceptibility to osteoporosis in postmenopausal
Japanese women.";
J. Bone Miner. Res. 13:1569-1576(1998).
[42]
VARIANTS CAEND CYS-218; HIS-218 AND ARG-225.
PubMed=10973241; DOI=10.1038/79128;
Kinoshita A., Saito T., Tomita H., Makita Y., Yoshida K., Ghadami M.,
Yamada K., Kondo S., Ikegawa S., Nishimura G., Fukushima Y.,
Nakagomi T., Saito H., Sugimoto T., Kamegaya M., Hisa K., Murray J.C.,
Taniguchi N., Niikawa N., Yoshiura K.;
"Domain-specific mutations in TGFB1 result in Camurati-Engelmann
disease.";
Nat. Genet. 26:19-20(2000).
[43]
VARIANTS CAEND HIS-81; CYS-218 AND ARG-225.
PubMed=11062463; DOI=10.1038/81563;
Janssens K., Gershoni-Baruch R., Guanabens N., Migone N., Ralston S.,
Bonduelle M., Lissens W., Van Maldergem L., Vanhoenacker F.,
Verbruggen L., Van Hul W.;
"Mutations in the gene encoding the latency-associated peptide of TGF-
beta 1 cause Camurati-Engelmann disease.";
Nat. Genet. 26:273-275(2000).
[44]
VARIANT PRO-10.
PubMed=12202987; DOI=10.1007/s100380200069;
Watanabe Y., Kinoshita A., Yamada T., Ohta T., Kishino T.,
Matsumoto N., Ishikawa M., Niikawa N., Yoshiura K.;
"A catalog of 106 single-nucleotide polymorphisms (SNPs) and 11 other
types of variations in genes for transforming growth factor-beta1
(TGF-beta1) and its signaling pathway.";
J. Hum. Genet. 47:478-483(2002).
[45]
CHARACTERIZATION OF VARIANTS CAEND HIS-81; CYS-218; ASP-222 AND
ARG-225.
PubMed=12493741; DOI=10.1074/jbc.m208857200;
Janssens K., ten Dijke P., Ralston S.H., Bergmann C., Van Hul W.;
"Transforming growth factor-beta-1 mutations in Camurati-Engelmann
disease lead to increased signaling by altering either activation or
secretion of the mutant protein.";
J. Biol. Chem. 278:7718-7724(2003).
[46]
CHARACTERIZATION OF VARIANT CAEND CYS-218.
PubMed=12843182; DOI=10.1210/jc.2002-020564;
McGowan N.W., MacPherson H., Janssens K., Van Hul W., Frith J.C.,
Fraser W.D., Ralston S.H., Helfrich M.H.;
"A mutation affecting the latency-associated peptide of TGFbeta1 in
Camurati-Engelmann disease enhances osteoclast formation in vitro.";
J. Clin. Endocrinol. Metab. 88:3321-3326(2003).
[47]
VARIANTS CAEND GLY-223 AND ARG-223.
PubMed=15103729; DOI=10.1002/ajmg.a.20671;
Kinoshita A., Fukumaki Y., Shirahama S., Miyahara A., Nishimura G.,
Haga N., Namba A., Ueda H., Hayashi H., Ikegawa S., Seidel J.,
Niikawa N., Yoshiura K.;
"TGFB1 mutations in four new families with Camurati-Engelmann disease:
confirmation of independently arising LAP-domain-specific mutations.";
Am. J. Med. Genet. 127A:104-107(2004).
-!- FUNCTION: Transforming growth factor beta-1 proprotein: Precursor
of the Latency-associated peptide (LAP) and Transforming growth
factor beta-1 (TGF-beta-1) chains, which constitute the regulatory
and active subunit of TGF-beta-1, respectively.
{ECO:0000269|PubMed:29109152, ECO:0000303|PubMed:27252363}.
-!- FUNCTION: Latency-associated peptide: Required to maintain the
Transforming growth factor beta-1 (TGF-beta-1) chain in a latent
state during storage in extracellular matrix (PubMed:28117447).
Associates non-covalently with TGF-beta-1 and regulates its
activation via interaction with 'milieu molecules', such as LTBP1,
LRRC32/GARP and LRRC33/NRROS, that control activation of TGF-beta-
1 (PubMed:2022183, PubMed:8617200, PubMed:8939931,
PubMed:19750484, PubMed:22278742, PubMed:19651619). Interaction
with LRRC33/NRROS regulates activation of TGF-beta-1 in
macrophages and microglia (Probable). Interaction with LRRC32/GARP
controls activation of TGF-beta-1 on the surface of activated
regulatory T-cells (Tregs) (PubMed:19750484, PubMed:22278742,
PubMed:19651619). Interaction with integrins (ITGAV:ITGB6 or
ITGAV:ITGB8) results in distortion of the Latency-associated
peptide chain and subsequent release of the active TGF-beta-1
(PubMed:22278742, PubMed:28117447). {ECO:0000269|PubMed:19651619,
ECO:0000269|PubMed:19750484, ECO:0000269|PubMed:2022183,
ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:28117447,
ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931,
ECO:0000305|PubMed:29909984}.
-!- FUNCTION: Transforming growth factor beta-1: Multifunctional
protein that regulates the growth and differentiation of various
cell types and is involved in various processes, such as normal
development, immune function, microglia function and responses to
neurodegeneration (By similarity). Activation into mature form
follows different steps: following cleavage of the proprotein in
the Golgi apparatus, Latency-associated peptide (LAP) and
Transforming growth factor beta-1 (TGF-beta-1) chains remain non-
covalently linked rendering TGF-beta-1 inactive during storage in
extracellular matrix (PubMed:29109152). At the same time, LAP
chain interacts with 'milieu molecules', such as LTBP1,
LRRC32/GARP and LRRC33/NRROS that control activation of TGF-beta-1
and maintain it in a latent state during storage in extracellular
milieus (PubMed:2022183, PubMed:8617200, PubMed:8939931,
PubMed:19750484, PubMed:22278742, PubMed:19651619). TGF-beta-1 is
released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8):
integrin-binding to LAP stabilizes an alternative conformation of
the LAP bowtie tail and results in distortion of the LAP chain and
subsequent release of the active TGF-beta-1 (PubMed:22278742,
PubMed:28117447). Once activated following release of LAP, TGF-
beta-1 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2),
which transduce signal (PubMed:20207738). While expressed by many
cells types, TGF-beta-1 only has a very localized range of action
within cell environment thanks to fine regulation of its
activation by Latency-associated peptide chain (LAP) and 'milieu
molecules' (By similarity). Plays an important role in bone
remodeling: acts as a potent stimulator of osteoblastic bone
formation, causing chemotaxis, proliferation and differentiation
in committed osteoblasts (By similarity). Can promote either T-
helper 17 cells (Th17) or regulatory T-cells (Treg) lineage
differentiation in a concentration-dependent manner (By
similarity). At high concentrations, leads to FOXP3-mediated
suppression of RORC and down-regulation of IL-17 expression,
favoring Treg cell development (By similarity). At low
concentrations in concert with IL-6 and IL-21, leads to expression
of the IL-17 and IL-23 receptors, favoring differentiation to Th17
cells (By similarity). Stimulates sustained production of collagen
through the activation of CREB3L1 by regulated intramembrane
proteolysis (RIP) (PubMed:25310401). Mediates SMAD2/3 activation
by inducing its phosphorylation and subsequent translocation to
the nucleus (PubMed:25893292, PubMed:29483653). Can induce
epithelial-to-mesenchymal transition (EMT) and cell migration in
various cell types (PubMed:25893292).
{ECO:0000250|UniProtKB:P04202, ECO:0000269|PubMed:19651619,
ECO:0000269|PubMed:19750484, ECO:0000269|PubMed:20207738,
ECO:0000269|PubMed:2022183, ECO:0000269|PubMed:22278742,
ECO:0000269|PubMed:25310401, ECO:0000269|PubMed:25893292,
ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152,
ECO:0000269|PubMed:29483653, ECO:0000269|PubMed:8617200,
ECO:0000269|PubMed:8939931}.
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:20207738,
PubMed:25209176, PubMed:28117447, PubMed:29109152). Interacts with
the serine proteases, HTRA1 and HTRA3: the interaction with either
inhibits TGFB1-mediated signaling. The HTRA protease activity is
required for this inhibition (By similarity). May interact with
THSD4; this interaction may lead to sequestration by FBN1
microfibril assembly and attenuation of TGFB signaling (By
similarity). Interacts with CD109, DPT and ASPN (PubMed:9895299,
PubMed:16754747, PubMed:17827158). Latency-associated peptide:
Homodimer; disulfide-linked (PubMed:28117447, PubMed:29109152).
Latency-associated peptide: Interacts with Transforming growth
factor beta-1 (TGF-beta-1) chain; interaction is non-covalent and
maintains (TGF-beta-1) in a latent state; each Latency-associated
peptide (LAP) monomer interacts with TGF-beta-1 in the other
monomer (PubMed:29109152). Latency-associated peptide: Interacts
with LTBP1; leading to regulate activation of TGF-beta-1
(PubMed:2022183, PubMed:8617200, PubMed:8939931). Latency-
associated peptide: Interacts with LRRC32/GARP; leading to
regulate activation of TGF-beta-1 on the surface of activated
regulatory T-cells (Tregs) (PubMed:19750484, PubMed:22278742,
PubMed:19651619). Interacts with LRRC33/NRROS; leading to regulate
activation of TGF-beta-1 in macrophages and microglia (Probable).
Latency-associated peptide: Interacts (via cell attachment site)
with integrins ITGAV and ITGB6 (ITGAV:ITGB6), leading to release
of the active TGF-beta-1 (PubMed:22278742, PubMed:28117447).
Latency-associated peptide: Interacts with NREP; the interaction
results in a decrease in TGFB1 autoinduction (By similarity).
Latency-associated peptide: Interacts with HSP90AB1; inhibits
latent TGFB1 activation (PubMed:20599762). Transforming growth
factor beta-1: Homodimer; disulfide-linked (PubMed:20207738,
PubMed:25209176, PubMed:28117447, PubMed:29109152). Transforming
growth factor beta-1: Interacts with TGF-beta receptors (TGFBR1
and TGFBR2), leading to signal transduction (PubMed:20207738).
{ECO:0000250|UniProtKB:P04202, ECO:0000269|PubMed:16754747,
ECO:0000269|PubMed:17827158, ECO:0000269|PubMed:19651619,
ECO:0000269|PubMed:19750484, ECO:0000269|PubMed:20207738,
ECO:0000269|PubMed:2022183, ECO:0000269|PubMed:20599762,
ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:25209176,
ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152,
ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931,
ECO:0000269|PubMed:9895299, ECO:0000305|PubMed:29909984}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-779636, EBI-779636;
P05067:APP; NbExp=3; IntAct=EBI-779636, EBI-77613;
Q14689:DIP2A; NbExp=2; IntAct=EBI-779636, EBI-2564275;
P17813:ENG; NbExp=2; IntAct=EBI-779636, EBI-2834630;
Q12841:FSTL1; NbExp=2; IntAct=EBI-779636, EBI-2349801;
Q14392:LRRC32; NbExp=2; IntAct=EBI-779636, EBI-15796956;
Q14766-1:LTBP1; NbExp=4; IntAct=EBI-779636, EBI-11173861;
P50222:MEOX2; NbExp=3; IntAct=EBI-779636, EBI-748397;
P11464:PSG1; NbExp=3; IntAct=EBI-779636, EBI-716740;
P36897:TGFBR1; NbExp=2; IntAct=EBI-779636, EBI-1027557;
P37173:TGFBR2; NbExp=6; IntAct=EBI-779636, EBI-296151;
Q03167:TGFBR3; NbExp=2; IntAct=EBI-779636, EBI-2852679;
Q90998:TGFBR3 (xeno); NbExp=2; IntAct=EBI-779636, EBI-6620843;
P07996:THBS1; NbExp=2; IntAct=EBI-779636, EBI-2530274;
-!- SUBCELLULAR LOCATION: Latency-associated peptide: Secreted,
extracellular space, extracellular matrix
{ECO:0000269|PubMed:17827158}.
-!- SUBCELLULAR LOCATION: Transforming growth factor beta-1: Secreted
{ECO:0000269|PubMed:17827158, ECO:0000269|PubMed:29483653}.
-!- TISSUE SPECIFICITY: Highly expressed in bone (PubMed:11746498,
PubMed:17827158). Abundantly expressed in articular cartilage and
chondrocytes and is increased in osteoarthritis (OA)
(PubMed:11746498, PubMed:17827158). Colocalizes with ASPN in
chondrocytes within OA lesions of articular cartilage
(PubMed:17827158). {ECO:0000269|PubMed:11746498,
ECO:0000269|PubMed:17827158}.
-!- DOMAIN: Latency-associated peptide: The 'straitjacket' and 'arm'
domains encircle the Transforming growth factor beta-1 (TGF-beta-
1) monomers and are fastened together by strong bonding between
Lys-56 and Tyr-103/Tyr-104. {ECO:0000250|UniProtKB:P07200}.
-!- DOMAIN: Latency-associated peptide: The cell attachment site motif
mediates binding to integrins (ITGAV:ITGB6 or ITGAV:ITGB8)
(PubMed:28117447). The motif locates to a long loop in the arm
domain called the bowtie tail (PubMed:28117447). Integrin-binding
stabilizes an alternative conformation of the bowtie tail
(PubMed:28117447). Activation by integrin requires force
application by the actin cytoskeleton, which is resisted by the
'milieu molecules' (such as LTBP1, LRRC32/GARP and/or
LRRC33/NRROS), resulting in distortion of the prodomain and
release of the active TGF-beta-1 (PubMed:28117447).
{ECO:0000269|PubMed:28117447}.
-!- PTM: Transforming growth factor beta-1 proprotein: The precursor
proprotein is cleaved in the Golgi apparatus by FURIN to form
Transforming growth factor beta-1 (TGF-beta-1) and Latency-
associated peptide (LAP) chains, which remain non-covalently
linked, rendering TGF-beta-1 inactive.
{ECO:0000269|PubMed:7737999}.
-!- PTM: Latency-associated peptide: N-glycosylated (PubMed:3162913,
PubMed:2493139, PubMed:28117447). Deglycosylation leads to
activation of Transforming growth factor beta-1 (TGF-beta-1);
mechanisms triggering deglycosylation-driven activation of TGF-
beta-1 are however unclear (PubMed:2493139).
{ECO:0000269|PubMed:2493139, ECO:0000269|PubMed:28117447,
ECO:0000269|PubMed:3162913}.
-!- POLYMORPHISM: In post-menopausal Japanese women, the frequency of
Leu-10 is higher in subjects with osteoporosis than in controls.
{ECO:0000269|PubMed:9783545}.
-!- DISEASE: Camurati-Engelmann disease (CAEND) [MIM:131300]: An
autosomal dominant disorder characterized by hyperostosis and
sclerosis of the diaphyses of long bones. The disease typically
presents in early childhood with pain, muscular weakness and
waddling gait, and in some cases other features such as
exophthalmos, facial paralysis, hearing difficulties and loss of
vision. {ECO:0000269|PubMed:10973241, ECO:0000269|PubMed:11062463,
ECO:0000269|PubMed:12493741, ECO:0000269|PubMed:12843182,
ECO:0000269|PubMed:15103729}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Inflammatory bowel disease, immunodeficiency, and
encephalopathy (IBDIMDE) [MIM:618213]: An autosomal recessive
disorder characterized by severe infantile inflammatory bowel
disease manifesting as bloody diarrhea and failure to thrive,
global developmental delay, epilepsy, brain atrophy and
encephalopathy. Affected individuals suffer from recurrent
infections associated with impaired T-cell response to stimulation
and decreased T-cell subsets, including regulatory and helper T
cells. {ECO:0000269|PubMed:29483653}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: TGF-beta-1 is inactivated by fresolimumab (also
named GC1008), a monoclonal-neutralizing antibody.
{ECO:0000269|PubMed:25209176}.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=TGF beta-1 entry;
URL="https://en.wikipedia.org/wiki/TGF_beta_1";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X05839; CAA29283.1; -; Genomic_DNA.
EMBL; X05840; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X05843; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X05844; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X05849; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X05850; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X02812; CAA26580.1; -; mRNA.
EMBL; BT007245; AAP35909.1; -; mRNA.
EMBL; AK291907; BAF84596.1; -; mRNA.
EMBL; CH471126; EAW57032.1; -; Genomic_DNA.
EMBL; BC001180; AAH01180.1; -; mRNA.
EMBL; BC000125; AAH00125.1; -; mRNA.
EMBL; BC022242; AAH22242.1; -; mRNA.
EMBL; M38449; AAA36735.1; -; mRNA.
CCDS; CCDS33031.1; -.
PIR; A27513; WFHU2.
RefSeq; NP_000651.3; NM_000660.6.
PDB; 1KLA; NMR; -; A/B=279-390.
PDB; 1KLC; NMR; -; A/B=279-390.
PDB; 1KLD; NMR; -; A/B=279-390.
PDB; 3KFD; X-ray; 3.00 A; A/B/C/D=279-390.
PDB; 4KV5; X-ray; 3.00 A; A/B/C/D=279-390.
PDB; 5FFO; X-ray; 3.49 A; C/D/G/H=34-390.
PDB; 5VQP; X-ray; 2.90 A; A=30-390.
PDBsum; 1KLA; -.
PDBsum; 1KLC; -.
PDBsum; 1KLD; -.
PDBsum; 3KFD; -.
PDBsum; 4KV5; -.
PDBsum; 5FFO; -.
PDBsum; 5VQP; -.
SMR; P01137; -.
BioGrid; 112898; 226.
ComplexPortal; CPX-529; TGF-beta-1-TGFR complex.
ComplexPortal; CPX-602; TGF-beta-1 complex.
CORUM; P01137; -.
DIP; DIP-5934N; -.
IntAct; P01137; 94.
MINT; P01137; -.
STRING; 9606.ENSP00000221930; -.
BindingDB; P01137; -.
ChEMBL; CHEMBL1795178; -.
DrugBank; DB10770; Foreskin fibroblast (neonatal).
DrugBank; DB10772; Foreskin keratinocyte (neonatal).
DrugBank; DB00070; Hyaluronidase (ovine).
DrugBank; DB01162; Terazosin.
DrugBank; DB06205; Vorhyaluronidase alfa.
GlyConnect; 1835; -.
iPTMnet; P01137; -.
PhosphoSitePlus; P01137; -.
BioMuta; TGFB1; -.
DMDM; 135674; -.
OGP; P01137; -.
EPD; P01137; -.
jPOST; P01137; -.
MassIVE; P01137; -.
MaxQB; P01137; -.
PaxDb; P01137; -.
PeptideAtlas; P01137; -.
PRIDE; P01137; -.
ProteomicsDB; 51337; -.
ABCD; P01137; -.
DNASU; 7040; -.
GeneID; 7040; -.
KEGG; hsa:7040; -.
UCSC; uc002oqh.4; human.
CTD; 7040; -.
DisGeNET; 7040; -.
GeneCards; TGFB1; -.
GeneReviews; TGFB1; -.
HGNC; HGNC:11766; TGFB1.
HPA; CAB000361; -.
HPA; CAB073543; -.
MalaCards; TGFB1; -.
MIM; 131300; phenotype.
MIM; 190180; gene.
MIM; 618213; phenotype.
neXtProt; NX_P01137; -.
Orphanet; 1328; Camurati-Engelmann disease.
Orphanet; 586; Cystic fibrosis.
PharmGKB; PA350; -.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
HOGENOM; HOG000290198; -.
InParanoid; P01137; -.
KO; K13375; -.
OrthoDB; 853728at2759; -.
PhylomeDB; P01137; -.
TreeFam; TF318514; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-168277; Influenza Virus Induced Apoptosis.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-3304356; SMAD2/3 Phosphorylation Motif Mutants in Cancer.
Reactome; R-HSA-3642279; TGFBR2 MSI Frameshift Mutants in Cancer.
Reactome; R-HSA-3645790; TGFBR2 Kinase Domain Mutants in Cancer.
Reactome; R-HSA-3656532; TGFBR1 KD Mutants in Cancer.
Reactome; R-HSA-3656535; TGFBR1 LBD Mutants in Cancer.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-8941855; RUNX3 regulates CDKN1A transcription.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
SignaLink; P01137; -.
SIGNOR; P01137; -.
ChiTaRS; TGFB1; human.
EvolutionaryTrace; P01137; -.
GeneWiki; TGF_beta_1; -.
GenomeRNAi; 7040; -.
Pharos; P01137; -.
PRO; PR:P01137; -.
Proteomes; UP000005640; Unplaced.
Bgee; ENSG00000105329; Expressed in 170 organ(s), highest expression level in leukocyte.
ExpressionAtlas; P01137; baseline and differential.
Genevisible; P01137; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0009986; C:cell surface; IMP:BHF-UCL.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0003823; F:antigen binding; IPI:UniProtKB.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IBA:GO_Central.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IMP:AgBase.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IDA:BHF-UCL.
GO; GO:0034714; F:type III transforming growth factor beta receptor binding; IMP:AgBase.
GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
GO; GO:0006754; P:ATP biosynthetic process; IDA:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
GO; GO:0048468; P:cell development; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0045216; P:cell-cell junction organization; IDA:BHF-UCL.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:BHF-UCL.
GO; GO:0002062; P:chondrocyte differentiation; IDA:UniProtKB.
GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IDA:UniProtKB.
GO; GO:0002248; P:connective tissue replacement involved in inflammatory response wound healing; TAS:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:1990402; P:embryonic liver development; ISS:BHF-UCL.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:UniProtKB.
GO; GO:0019049; P:evasion or tolerance of host defenses by virus; IDA:BHF-UCL.
GO; GO:0085029; P:extracellular matrix assembly; IDA:BHF-UCL.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0007507; P:heart development; ISS:BHF-UCL.
GO; GO:0003179; P:heart valve morphogenesis; ISS:BHF-UCL.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IDA:UniProtKB.
GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0048535; P:lymph node development; ISS:UniProtKB.
GO; GO:0010742; P:macrophage derived foam cell differentiation; IC:BHF-UCL.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IDA:UniProtKB.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IDA:BHF-UCL.
GO; GO:0070168; P:negative regulation of biomineral tissue development; IDA:BHF-UCL.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0045786; P:negative regulation of cell cycle; IDA:HGNC.
GO; GO:0045596; P:negative regulation of cell differentiation; IEP:CACAO.
GO; GO:0030308; P:negative regulation of cell growth; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:BHF-UCL.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0045918; P:negative regulation of cytolysis; IDA:ARUK-UCL.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:BHF-UCL.
GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; IC:BHF-UCL.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
GO; GO:0060965; P:negative regulation of gene silencing by miRNA; IGI:BHF-UCL.
GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; IDA:UniProtKB.
GO; GO:0010936; P:negative regulation of macrophage cytokine production; IDA:DFLAT.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:BHF-UCL.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IDA:UniProtKB.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; IGI:BHF-UCL.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0001843; P:neural tube closure; ISS:BHF-UCL.
GO; GO:0021915; P:neural tube development; ISS:BHF-UCL.
GO; GO:0043932; P:ossification involved in bone remodeling; IEP:BHF-UCL.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:UniProtKB.
GO; GO:0006796; P:phosphate-containing compound metabolic process; IDA:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0030501; P:positive regulation of bone mineralization; IEP:BHF-UCL.
GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; IDA:BHF-UCL.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IDA:BHF-UCL.
GO; GO:0050921; P:positive regulation of chemotaxis; IDA:BHF-UCL.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:1901203; P:positive regulation of extracellular matrix assembly; IC:BHF-UCL.
GO; GO:0010763; P:positive regulation of fibroblast migration; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; IDA:MGI.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
GO; GO:0014008; P:positive regulation of microglia differentiation; ISS:UniProtKB.
GO; GO:1901666; P:positive regulation of NAD+ ADP-ribosyltransferase activity; IDA:BHF-UCL.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:BHF-UCL.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0031334; P:positive regulation of protein complex assembly; IDA:BHF-UCL.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:BHF-UCL.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0050714; P:positive regulation of protein secretion; IDA:BHF-UCL.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:BHF-UCL.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; TAS:BHF-UCL.
GO; GO:0043117; P:positive regulation of vascular permeability; IDA:UniProtKB.
GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0032801; P:receptor catabolic process; IDA:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0051098; P:regulation of binding; ISS:UniProtKB.
GO; GO:0060312; P:regulation of blood vessel remodeling; NAS:BHF-UCL.
GO; GO:0030334; P:regulation of cell migration; TAS:BHF-UCL.
GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
GO; GO:0051101; P:regulation of DNA binding; ISS:UniProtKB.
GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0042306; P:regulation of protein import into nucleus; ISS:UniProtKB.
GO; GO:0060390; P:regulation of SMAD protein signal transduction; IDA:UniProtKB.
GO; GO:0016202; P:regulation of striated muscle tissue development; ISS:UniProtKB.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0070723; P:response to cholesterol; IDA:BHF-UCL.
GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL.
GO; GO:0032570; P:response to progesterone; IDA:BHF-UCL.
GO; GO:0009611; P:response to wounding; IEP:BHF-UCL.
GO; GO:0007435; P:salivary gland morphogenesis; IEP:BHF-UCL.
GO; GO:0007183; P:SMAD protein complex assembly; IDA:BHF-UCL.
GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:1905313; P:transforming growth factor beta receptor signaling pathway involved in heart development; ISS:BHF-UCL.
GO; GO:0001570; P:vasculogenesis; ISS:BHF-UCL.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR016319; TGF-beta.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR003939; TGFb1.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
PIRSF; PIRSF001787; TGF-beta; 1.
PRINTS; PR01423; TGFBETA.
PRINTS; PR01424; TGFBETA1.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Extracellular matrix; Glycoprotein; Growth factor; Mitogen;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 29 {ECO:0000269|PubMed:3162913}.
CHAIN 30 278 Latency-associated peptide.
{ECO:0000305|PubMed:2982829,
ECO:0000305|PubMed:3162913,
ECO:0000305|PubMed:7737999,
ECO:0000305|PubMed:8471846}.
/FTId=PRO_0000033762.
CHAIN 279 390 Transforming growth factor beta-1.
{ECO:0000305|PubMed:2982829,
ECO:0000305|PubMed:3162913,
ECO:0000305|PubMed:7737999,
ECO:0000305|PubMed:8471846}.
/FTId=PRO_0000033763.
REGION 30 74 Straightjacket domain.
{ECO:0000250|UniProtKB:P07200}.
REGION 75 271 Arm domain.
{ECO:0000250|UniProtKB:P07200}.
REGION 226 252 Bowtie tail.
{ECO:0000269|PubMed:28117447}.
MOTIF 244 246 Cell attachment site.
{ECO:0000269|PubMed:28117447}.
SITE 278 279 Cleavage; by FURIN.
{ECO:0000269|PubMed:7737999}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5FFO,
ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:28117447}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 33 33 Interchain (with C-1359 or C-1384 in
LTBP1); in inactive form.
{ECO:0000305|PubMed:22278742}.
DISULFID 223 223 Interchain (with C-225).
{ECO:0000244|PDB:5FFO,
ECO:0000244|PDB:5VQP,
ECO:0000269|PubMed:28117447,
ECO:0000269|PubMed:29109152}.
DISULFID 225 225 Interchain (with C-223).
{ECO:0000244|PDB:5FFO,
ECO:0000244|PDB:5VQP,
ECO:0000269|PubMed:28117447,
ECO:0000269|PubMed:29109152}.
DISULFID 285 294 {ECO:0000244|PDB:3KFD,
ECO:0000244|PDB:4KV5,
ECO:0000244|PDB:5FFO,
ECO:0000244|PDB:5VQP,
ECO:0000269|PubMed:20207738,
ECO:0000269|PubMed:25209176,
ECO:0000269|PubMed:28117447,
ECO:0000269|PubMed:29109152}.
DISULFID 293 356 {ECO:0000244|PDB:3KFD,
ECO:0000244|PDB:4KV5,
ECO:0000244|PDB:5FFO,
ECO:0000244|PDB:5VQP,
ECO:0000269|PubMed:20207738,
ECO:0000269|PubMed:25209176,
ECO:0000269|PubMed:28117447,
ECO:0000269|PubMed:29109152}.
DISULFID 322 387 {ECO:0000244|PDB:3KFD,
ECO:0000244|PDB:4KV5,
ECO:0000244|PDB:5FFO,
ECO:0000244|PDB:5VQP,
ECO:0000269|PubMed:20207738,
ECO:0000269|PubMed:25209176,
ECO:0000269|PubMed:28117447,
ECO:0000269|PubMed:29109152}.
DISULFID 326 389 {ECO:0000244|PDB:3KFD,
ECO:0000244|PDB:4KV5,
ECO:0000244|PDB:5FFO,
ECO:0000244|PDB:5VQP,
ECO:0000269|PubMed:20207738,
ECO:0000269|PubMed:25209176,
ECO:0000269|PubMed:28117447,
ECO:0000269|PubMed:29109152}.
DISULFID 355 355 Interchain. {ECO:0000244|PDB:3KFD,
ECO:0000244|PDB:4KV5,
ECO:0000244|PDB:5FFO,
ECO:0000269|PubMed:20207738,
ECO:0000269|PubMed:25209176,
ECO:0000269|PubMed:28117447}.
VARIANT 10 10 L -> P (associated with higher bone
mineral density and lower frequency of
vertebral fractures in Japanese post-
menopausal women; dbSNP:rs1800470).
{ECO:0000269|PubMed:12202987,
ECO:0000269|PubMed:3861940,
ECO:0000269|PubMed:9783545}.
/FTId=VAR_016171.
VARIANT 25 25 R -> P (in dbSNP:rs1800471).
{ECO:0000269|PubMed:3861940}.
/FTId=VAR_016172.
VARIANT 45 45 R -> C (in IBDIMDE; decreased TGFB1-
mediated activation of SMAD signaling;
reduced levels of secreated TGFB1).
{ECO:0000269|PubMed:29483653}.
/FTId=VAR_081584.
VARIANT 81 81 Y -> H (in CAEND; leads to TGF-beta-1
intracellular accumulation).
{ECO:0000269|PubMed:11062463,
ECO:0000269|PubMed:12493741}.
/FTId=VAR_017607.
VARIANT 110 110 R -> C (in IBDIMDE; decreased TGFB1-
mediated activation of SMAD signaling;
reduced levels of secreated TGFB1).
{ECO:0000269|PubMed:29483653}.
/FTId=VAR_081585.
VARIANT 218 218 R -> C (in CAEND; higher levels of active
TGF-beta-1 in the culture medium;
enhances osteoclast formation in vitro).
{ECO:0000269|PubMed:10973241,
ECO:0000269|PubMed:11062463,
ECO:0000269|PubMed:12493741,
ECO:0000269|PubMed:12843182}.
/FTId=VAR_017608.
VARIANT 218 218 R -> H (in CAEND).
{ECO:0000269|PubMed:10973241}.
/FTId=VAR_017609.
VARIANT 222 222 H -> D (in CAEND; sporadic case; higher
levels of active TGF-beta-1 in the
culture medium).
{ECO:0000269|PubMed:12493741}.
/FTId=VAR_017610.
VARIANT 223 223 C -> G (in CAEND).
{ECO:0000269|PubMed:15103729}.
/FTId=VAR_067303.
VARIANT 223 223 C -> R (in CAEND).
{ECO:0000269|PubMed:15103729}.
/FTId=VAR_067304.
VARIANT 225 225 C -> R (in CAEND; higher levels of active
TGF-beta-1 in the culture medium).
{ECO:0000269|PubMed:10973241,
ECO:0000269|PubMed:11062463,
ECO:0000269|PubMed:12493741}.
/FTId=VAR_017611.
VARIANT 263 263 T -> I (in dbSNP:rs1800472).
/FTId=VAR_016173.
VARIANT 387 387 C -> R (in IBDIMDE; loss of TGFB1-
mediated activation of SMAD signaling;
mutant TGFB1 is not secreted).
{ECO:0000269|PubMed:29483653}.
/FTId=VAR_081586.
MUTAGEN 33 33 C->S: Abolishes interchain disulfide bond
with LTBP1 and/or LRRC32, and subsequent
regulation of activation of TGF-beta-1.
{ECO:0000269|PubMed:22278742,
ECO:0000269|PubMed:8617200}.
MUTAGEN 75 75 E->A: Does not affect integrin-binding or
activation of TGF-beta-1.
{ECO:0000269|PubMed:28117447}.
MUTAGEN 158 158 L->A: Does not affect integrin-binding or
activation of TGF-beta-1.
{ECO:0000269|PubMed:28117447}.
MUTAGEN 160 160 L->A,R: Does not affect integrin-binding
or activation of TGF-beta-1.
{ECO:0000269|PubMed:28117447}.
MUTAGEN 193 193 P->A,R: Does not affect integrin-binding
or activation of TGF-beta-1.
{ECO:0000269|PubMed:28117447}.
MUTAGEN 232 236 LQVDI->GQGDG: Strongly inhibits integrin-
binding and activation of TGF-beta-1.
{ECO:0000269|PubMed:28117447}.
MUTAGEN 234 236 VDI->GDG: Strongly inhibits integrin-
binding and activation of TGF-beta-1.
{ECO:0000269|PubMed:28117447}.
MUTAGEN 237 237 N->A: Does not affect integrin-binding or
activation of TGF-beta-1.
{ECO:0000269|PubMed:28117447}.
MUTAGEN 254 254 N->A: Does not affect integrin-binding or
activation of TGF-beta-1.
{ECO:0000269|PubMed:28117447}.
MUTAGEN 257 260 FLLL->GLLG: Strongly inhibits integrin-
binding and activation of TGF-beta-1.
{ECO:0000269|PubMed:28117447}.
MUTAGEN 278 278 R->A: Prevents cleavage and subsequent
maturation of the protein. Generated in
order to mimic the structure of the
Transforming growth factor beta-1
proprotein.
{ECO:0000269|PubMed:29109152}.
CONFLICT 159 159 R -> RR (in Ref. 2; CAA26580).
{ECO:0000305}.
HELIX 33 57 {ECO:0000244|PDB:5VQP}.
STRAND 70 72 {ECO:0000244|PDB:5FFO}.
HELIX 75 85 {ECO:0000244|PDB:5VQP}.
STRAND 107 112 {ECO:0000244|PDB:5VQP}.
TURN 123 126 {ECO:0000244|PDB:5VQP}.
STRAND 130 136 {ECO:0000244|PDB:5VQP}.
HELIX 137 143 {ECO:0000244|PDB:5VQP}.
STRAND 144 146 {ECO:0000244|PDB:5FFO}.
HELIX 147 149 {ECO:0000244|PDB:5VQP}.
STRAND 150 159 {ECO:0000244|PDB:5VQP}.
STRAND 166 174 {ECO:0000244|PDB:5VQP}.
TURN 175 177 {ECO:0000244|PDB:5VQP}.
STRAND 178 187 {ECO:0000244|PDB:5VQP}.
STRAND 194 199 {ECO:0000244|PDB:5VQP}.
HELIX 201 209 {ECO:0000244|PDB:5VQP}.
STRAND 213 228 {ECO:0000244|PDB:5VQP}.
STRAND 231 238 {ECO:0000244|PDB:5VQP}.
STRAND 242 244 {ECO:0000244|PDB:5FFO}.
TURN 245 247 {ECO:0000244|PDB:5VQP}.
STRAND 251 254 {ECO:0000244|PDB:5VQP}.
STRAND 257 262 {ECO:0000244|PDB:5VQP}.
HELIX 265 268 {ECO:0000244|PDB:5VQP}.
TURN 282 284 {ECO:0000244|PDB:1KLC}.
HELIX 285 288 {ECO:0000244|PDB:5VQP}.
STRAND 290 301 {ECO:0000244|PDB:5VQP}.
TURN 302 305 {ECO:0000244|PDB:5VQP}.
STRAND 311 313 {ECO:0000244|PDB:5VQP}.
STRAND 315 323 {ECO:0000244|PDB:5VQP}.
STRAND 330 332 {ECO:0000244|PDB:3KFD}.
HELIX 335 346 {ECO:0000244|PDB:3KFD}.
STRAND 347 349 {ECO:0000244|PDB:3KFD}.
STRAND 350 353 {ECO:0000244|PDB:5FFO}.
STRAND 355 370 {ECO:0000244|PDB:5VQP}.
STRAND 373 390 {ECO:0000244|PDB:5VQP}.
SEQUENCE 390 AA; 44341 MW; 75391614250288FE CRC64;
MPPSGLRLLL LLLPLLWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR GQILSKLRLA
SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESAEPEPEPE ADYYAKEVTR VLMVETHNEI
YDKFKQSTHS IYMFFNTSEL REAVPEPVLL SRAELRLLRL KLKVEQHVEL YQKYSNNSWR
YLSNRLLAPS DSPEWLSFDV TGVVRQWLSR GGEIEGFRLS AHCSCDSRDN TLQVDINGFT
TGRRGDLATI HGMNRPFLLL MATPLERAQH LQSSRHRRAL DTNYCFSSTE KNCCVRQLYI
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SAAPCCVPQA
LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS


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[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFBR1 ALK5 SKR4] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Activin A receptor type II-like protein kinase of 53kD) (Activin receptor-like kinase 5) (ALK-5) (ALK5) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr3] Transforming growth factor beta receptor type 3 (TGF-beta receptor type 3) (TGFR-3) (Betaglycan) (Transforming growth factor beta receptor III) (TGF-beta receptor type III)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (ESK2) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Lefty1 Ebaf Lefty Stra3 Tgfb4] Left-right determination factor 1 (Protein lefty-1) (Lefty protein) (Stimulated by retinoic acid gene 3 protein) (Transforming growth factor beta-4) (TGF-beta-4)
[TGFBR2] TGF-beta receptor type-2 (TGFR-2) (EC 2.7.11.30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II) (TGF-beta receptor type II) (TbetaR-II)
[MAP3K7 TAK1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[Map3k7 Tak1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[LEFTY2 EBAF LEFTA LEFTYA TGFB4 PSEC0024] Left-right determination factor 2 (Endometrial bleeding-associated factor) (Left-right determination factor A) (Protein lefty-2) (Protein lefty-A) (Transforming growth factor beta-4) (TGF-beta-4)
[Nrros Lrrc33] Transforming growth factor beta activator LRRC33 (Leucine-rich repeat-containing protein 33) (Negative regulator of reactive oxygen species)
[LTBP4] Latent-transforming growth factor beta-binding protein 4 (LTBP-4)
[tgfb1] Transforming growth factor beta-1 proprotein (TGF-beta-5) [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGF beta TGFB1] Transforming growth factor beta

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